TY - JOUR
T1 - Activation of Pyrococcus furiosus alkaline phosphatase by divalent metal ions
AU - Minamihata, Kosuke
AU - Goto, Masahiro
AU - Kamiya, Noriho
N1 - Funding Information:
Acknowledgments This work was supported in part by the Science and Technology Incubation Program in Advanced Regions from the Japan Science and Technology Agency (JST). K. Minamihata was supported by a Research Fellowship of the Japan Society for the Promotion of Science (JSPS) for young scientists.
PY - 2012/10
Y1 - 2012/10
N2 - Treatment of a hyperthermophilic enzyme, alkaline phosphatase from Pyrococcus furiosus (PfuAP), with EDTA completely deactivated PfuAP, indicating that the presence of one or more divalent metal ions is essential for its catalytic activity. Subsequent addition of various divalent metal ions to the apoprotein recovered the enzymatic activity and, in particular, the addition of Co(II) resulted in an over 50-fold increase in activity compared with PfuAP before EDTA treatment. Intriguingly, PfuAP with Co(II) exhibited weaker stability toward heat treatment, suggesting that Co2+ destabilizes the tertiary structure of PfuAP at high temperature.
AB - Treatment of a hyperthermophilic enzyme, alkaline phosphatase from Pyrococcus furiosus (PfuAP), with EDTA completely deactivated PfuAP, indicating that the presence of one or more divalent metal ions is essential for its catalytic activity. Subsequent addition of various divalent metal ions to the apoprotein recovered the enzymatic activity and, in particular, the addition of Co(II) resulted in an over 50-fold increase in activity compared with PfuAP before EDTA treatment. Intriguingly, PfuAP with Co(II) exhibited weaker stability toward heat treatment, suggesting that Co2+ destabilizes the tertiary structure of PfuAP at high temperature.
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U2 - 10.1007/s10529-012-0998-0
DO - 10.1007/s10529-012-0998-0
M3 - Article
C2 - 22777300
AN - SCOPUS:84867099597
SN - 0141-5492
VL - 34
SP - 2055
EP - 2060
JO - Biotechnology Letters
JF - Biotechnology Letters
IS - 11
ER -